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6841486 
Journal Article 
Hydrodynamic characterization of Chromobacter viscosum lipase 
Simpkin, N; Food Sci, U; Harding, SE; Tombs, MP 
1990 
18 
5 
1031-1031 
In this study, we consider the hydrodynamic properties of the lipase from Chromobacter viscosum in term of molecular mass in solution and sedimentation velocity behaviour. It has been the particular intention of this study to examine the possibility of self-association for C. viscosum lipase. Taken in isolation these results appear to indicate that C. viscosum lipase has a molecular mass of 38,000 plus or minus 2000. Some self-association behaviour, although the absence of an observed decrease in M super(0) sub(r),wf)or the 1,4-dioxane and low-temperature buffer systems would appear to suggest that the association, if present, is not hydrophobic in nature. 
sedimentation hydrodynamics lipase